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The Major Capsid Protein, VP1, of the Mouse Polyomavirus Stimulates the Activity of Tubulin Acetyltransferase 1 by Microtubule Stabilization
L. Horníková, K. Bruštíková, B. Ryabchenko, I. Zhernov, M. Fraiberk, Z. Mariničová, Z. Lánský, J. Forstová
Jazyk angličtina Země Švýcarsko
Typ dokumentu časopisecké články, práce podpořená grantem
Free Medical Journals od 2009
PubMed Central od 2009
Europe PubMed Central od 2009
ProQuest Central od 2009-01-01
Open Access Digital Library od 2009-01-01
Open Access Digital Library od 2009-01-01
Health & Medicine (ProQuest) od 2009-01-01
ROAD: Directory of Open Access Scholarly Resources od 2009
Odkazy
PubMed
32085463
DOI
10.3390/v12020227
Knihovny.cz E-zdroje
- MeSH
- acetylace MeSH
- acetyltransferasy genetika metabolismus MeSH
- buněčné linie MeSH
- buněčný cyklus MeSH
- cytoplazma metabolismus MeSH
- fibroblasty virologie MeSH
- histondeacetylasa 6 genetika metabolismus MeSH
- interakce mikroorganismu a hostitele * MeSH
- mikrotubuly metabolismus virologie MeSH
- myši MeSH
- Polyomavirus genetika metabolismus MeSH
- posttranslační úpravy proteinů MeSH
- tubulin metabolismus MeSH
- virové plášťové proteiny genetika metabolismus MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Viruses have evolved mechanisms to manipulate microtubules (MTs) for the efficient realization of their replication programs. Studying the mechanisms of replication of mouse polyomavirus (MPyV), we observed previously that in the late phase of infection, a considerable amount of the main structural protein, VP1, remains in the cytoplasm associated with hyperacetylated microtubules. VP1-microtubule interactions resulted in blocking the cell cycle in the G2/M phase. We are interested in the mechanism leading to microtubule hyperacetylation and stabilization and the roles of tubulin acetyltransferase 1 (αTAT1) and deacetylase histone deacetylase 6 (HDAC6) and VP1 in this mechanism. Therefore, HDAC6 inhibition assays, αTAT1 knock out cell infections, in situ cell fractionation, and confocal and TIRF microscopy were used. The experiments revealed that the direct interaction of isolated microtubules and VP1 results in MT stabilization and a restriction of their dynamics. VP1 leads to an increase in polymerized tubulin in cells, thus favoring αTAT1 activity. The acetylation status of MTs did not affect MPyV infection. However, the stabilization of MTs by VP1 in the late phase of infection may compensate for the previously described cytoskeleton destabilization by MPyV early gene products and is important for the observed inhibition of the G2→M transition of infected cells to prolong the S phase.
Faculty of Mathematics and Physics Charles University 12844 Prague Czech Republic
Institute of Biotechnology of the Czech Academy of Sciences BIOCEV 25250 Vestec Czech Republic
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- $a Viruses have evolved mechanisms to manipulate microtubules (MTs) for the efficient realization of their replication programs. Studying the mechanisms of replication of mouse polyomavirus (MPyV), we observed previously that in the late phase of infection, a considerable amount of the main structural protein, VP1, remains in the cytoplasm associated with hyperacetylated microtubules. VP1-microtubule interactions resulted in blocking the cell cycle in the G2/M phase. We are interested in the mechanism leading to microtubule hyperacetylation and stabilization and the roles of tubulin acetyltransferase 1 (αTAT1) and deacetylase histone deacetylase 6 (HDAC6) and VP1 in this mechanism. Therefore, HDAC6 inhibition assays, αTAT1 knock out cell infections, in situ cell fractionation, and confocal and TIRF microscopy were used. The experiments revealed that the direct interaction of isolated microtubules and VP1 results in MT stabilization and a restriction of their dynamics. VP1 leads to an increase in polymerized tubulin in cells, thus favoring αTAT1 activity. The acetylation status of MTs did not affect MPyV infection. However, the stabilization of MTs by VP1 in the late phase of infection may compensate for the previously described cytoskeleton destabilization by MPyV early gene products and is important for the observed inhibition of the G2→M transition of infected cells to prolong the S phase.
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